Evidence map›Paper›PMID 41022877›Full record

ArticleNature communications2025

A robust platform streamlining aromatic noncanonical amino acid biosynthesis and genetic code expansion in Escherichia coli.

Jingxuan Zhang, Keying Yu, Yali Xu, Wushuang Zhao, Yulian Li, Ying Wang, Florian P Seebeck, Xiao-Hua Chen, Cangsong Liao

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Jingxuan Zhang *State Key Laboratory of Chemical Biology, Shanghai Institute of Material Medica, Chinese Academy of Sciences, Shanghai, China.
Keying Yu *State Key Laboratory of Chemical Biology, Shanghai Institute of Material Medica, Chinese Academy of Sciences, Shanghai, China.
Yali Xu *State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Wushuang ZhaoState Key Laboratory of Chemical Biology, Shanghai Institute of Material Medica, Chinese Academy of Sciences, Shanghai, China.
Yulian LiState Key Laboratory of Chemical Biology, Shanghai Institute of Material Medica, Chinese Academy of Sciences, Shanghai, China.
Ying WangState Key Laboratory of Synthetic Biology, Tianjin University, Tianjin, China.
Florian P SeebeckDepartment for Chemistry, University of Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0003-4625-1369
Xiao-Hua ChenState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. xhchen@simm.ac.cn.ORCID http://orcid.org/0000-0003-3031-7095
Cangsong LiaoState Key Laboratory of Chemical Biology, Shanghai Institute of Material Medica, Chinese Academy of Sciences, Shanghai, China. csliao@simm.ac.cn.ORCID http://orcid.org/0000-0003-4667-7407

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22071259National Natural Science Foundation of China (National Science Foundation of China) 22307126Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 206039
6 · The paper itself

Abstract

Genetic code expansion (GCE) has significantly enhanced the diversity of proteins in the biological world, leading to a wide range of applications. Despite the advances in GCE, the cost of noncanonical amino acids (ncAAs) remains one of the major obstacles for large-scale production. In situ biosynthesis of ncAAs from commercial precursors offers a promising solution to this challenge, yet only a few biosynthetic pathways have been reported. Here, we present a platform that couples the biosynthesis of aromatic ncAAs with genetic code expansion in E. coli, enabling the production of proteins and peptides containing ncAAs. Forty ncAAs are synthesized from aryl aldehydes by the biosynthetic pathway, while nineteen ncAAs are incorporated into superfolder GFP using three orthogonal translation systems. The platform's versatility is demonstrated by the production of macrocyclic peptides and antibody fragments. We envision that the platform will facilitate the production of peptides, enzymes, and antibody fragments containing ncAAs.

Indexed as

Amino AcidsAmino Acids, AromaticEscherichia coliGenetic CodeBiosynthetic PathwaysGreen Fluorescent ProteinsMetabolic EngineeringPeptidesProtein BiosynthesisAmino AcidsAmino Acids, AromaticGreen Fluorescent ProteinsPeptides

Identifiers

PMID41022877
PMCPMC12480666

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.